This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1hk7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 24: Line 24:
[[Category: heat shock protein]]
[[Category: heat shock protein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:47:30 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:37:31 2007''

Revision as of 13:32, 30 October 2007

Image:1hk7.gif

1hk7, resolution 2.50Å

Drag the structure with the mouse to rotate

MIDDLE DOMAIN OF HSP90

Overview

Activation of client proteins by the Hsp90 molecular chaperone is, dependent on binding and hydrolysis of ATP, which drives a molecular clamp, via transient dimerization of the N-terminal domains. The crystal, structure of the middle segment of yeast Hsp90 reveals considerable, evolutionary divergence from the equivalent regions of other GHKL protein, family members such as MutL and GyrB, including an additional domain of, new fold. Using the known structure of the N-terminal nucleotide binding, domain, a model for the Hsp90 dimer has been constructed. From this, structure, residues implicated in the ATPase-coupled conformational cycle, and in interactions with client proteins and the activating cochaperone, Aha1 have been identified, and their roles functionally characterized in, vitro ... [(full description)]

About this Structure

1HK7 is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with CD and MG as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions., Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH, Mol Cell. 2003 Mar;11(3):647-58. PMID:12667448

Page seeded by OCA on Tue Oct 30 15:37:31 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hk7"
Personal tools